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Solute carrier family 22 member 1 (Organic cation transporter 1) (hOCT1)

 S22A1_HUMAN             Reviewed;         554 AA.
O15245; A6NFF3; A8K1H2; C9JSU6; O15395; Q9NQD4;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 2.
25-OCT-2017, entry version 150.
RecName: Full=Solute carrier family 22 member 1;
AltName: Full=Organic cation transporter 1;
Short=hOCT1;
Name=SLC22A1; Synonyms=OCT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND VARIANT PHE-160.
TISSUE=Liver;
PubMed=9260930; DOI=10.1089/dna.1997.16.871;
Gorboulev V., Ulzheimer J.C., Akhoundova A., Ulzheimer-Teuber I.,
Karbach U., Quester S., Baumann C., Lang F., Busch A.E., Koepsell H.;
"Cloning and characterization of two human polyspecific organic cation
transporters.";
DNA Cell Biol. 16:871-881(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
PROPERTIES, AND TISSUE SPECIFICITY.
PubMed=9187257;
Zhang L., Dresser M.J., Gray A.T., Yost S.C., Terashita S.,
Giacomini K.M.;
"Cloning and functional expression of a human liver organic cation
transporter.";
Mol. Pharmacol. 51:913-921(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, TISSUE
SPECIFICITY, AND ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4).
PubMed=11388889; DOI=10.1046/j.1469-1809.2000.6430267.x;
Hayer M., Boenisch H., Bruess M.;
"Molecular cloning, functional characterization and genomic
organization of four alternatively spliced isoforms of the human
organic cation transporter 1 (hOCT1/SLC22A1).";
Ann. Hum. Genet. 63:473-482(1999).
[4]
ERRATUM, AND SEQUENCE REVISION.
Hayer M., Bonisch H., Bruss M.;
Ann. Hum. Genet. 64:267-267(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
PHE-160; VAL-408; MET-420 DEL AND ARG-465.
TISSUE=Caudate nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
PHE-160.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9655880;
Zhang L., Schaner M.E., Giacomini K.M.;
"Functional characterization of an organic cation transporter (hOCT1)
in a transiently transfected human cell line (HeLa).";
J. Pharmacol. Exp. Ther. 286:354-361(1998).
[9]
FUNCTION.
PubMed=11408531;
van Montfoort J.E., Mueller M., Groothuis G.M.M., Meijer D.K.F.,
Koepsell H., Meier P.J.;
"Comparison of 'type I' and 'type II' organic cation transport by
organic cation transporters and organic anion-transporting
polypeptides.";
J. Pharmacol. Exp. Ther. 298:110-115(2001).
[10]
FUNCTION.
PubMed=15389554; DOI=10.1002/jcp.20081;
Ciarimboli G., Struwe K., Arndt P., Gorboulev V., Koepsell H.,
Schlatter E., Hirsch J.R.;
"Regulation of the human organic cation transporter hOCT1.";
J. Cell. Physiol. 201:420-428(2004).
[11]
SUBCELLULAR LOCATION.
PubMed=16263091; DOI=10.1016/j.bcp.2005.09.011;
Mueller J., Lips K.S., Metzner L., Neubert R.H.H., Koepsell H.,
Brandsch M.;
"Drug specificity and intestinal membrane localization of human
organic cation transporters (OCT).";
Biochem. Pharmacol. 70:1851-1860(2005).
[12]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16272756; DOI=10.2133/dmpk.20.379;
Kimura N., Masuda S., Tanihara Y., Ueo H., Okuda M., Katsura T.,
Inui K.;
"Metformin is a superior substrate for renal organic cation
transporter OCT2 rather than hepatic OCT1.";
Drug Metab. Pharmacokinet. 20:379-386(2005).
[13]
INDUCTION.
PubMed=16436500; DOI=10.1124/jpet.105.099929;
Saborowski M., Kullak-Ublick G.A., Eloranta J.J.;
"The human organic cation transporter-1 gene is transactivated by
hepatocyte nuclear factor-4alpha.";
J. Pharmacol. Exp. Ther. 317:778-785(2006).
[14]
FUNCTION.
PubMed=16581093; DOI=10.1016/j.neuropharm.2006.01.005;
Amphoux A., Vialou V., Drescher E., Bruess M., Mannoury La Cour C.,
Rochat C., Millan M.J., Giros B., Boenisch H., Gautron S.;
"Differential pharmacological in vitro properties of organic cation
transporters and regional distribution in rat brain.";
Neuropharmacology 50:941-952(2006).
[15]
INDUCTION.
PubMed=17635184; DOI=10.1111/j.1472-8206.2007.00517.x;
Dias V., Ribeiro V.;
"The expression of the solute carriers NTCP and OCT-1 is regulated by
cholesterol in HepG2 cells.";
Fundam. Clin. Pharmacol. 21:445-450(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-541, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
VARIANTS CYS-61; ARG-88; PHE-160; SER-401 AND MET-420 DEL, AND
CHARACTERIZATION OF VARIANTS CYS-61; ARG-88; PHE-160; SER-401 AND
MET-420 DEL.
PubMed=12439218; DOI=10.1097/00008571-200211000-00002;
Kerb R., Brinkmann U., Chatskaia N., Gorbunov D., Gorboulev V.,
Mornhinweg E., Keil A., Eichelbaum M., Koepsell H.;
"Identification of genetic variations of the human organic cation
transporter hOCT1 and their functional consequences.";
Pharmacogenetics 12:591-595(2002).
[18]
VARIANTS PHE-14; CYS-61; PHE-85; PHE-160; LEU-189; VAL-220; LEU-341;
HIS-342; SER-401; VAL-408; MET-420 DEL; ILE-440; ILE-461; ARG-465 AND
MET-488, CHARACTERIZATION OF VARIANTS PHE-14; CYS-61; PHE-85; PHE-160;
LEU-189; VAL-220; LEU-341; HIS-342; SER-401; VAL-408; MET-420 DEL;
ILE-440; ILE-461; ARG-465 AND MET-488, AND MUTAGENESIS OF GLY-465.
PubMed=12719534; DOI=10.1073/pnas.0730858100;
Shu Y., Leabman M.K., Feng B., Mangravite L.M., Huang C.C., Stryke D.,
Kawamoto M., Johns S.J., DeYoung J., Carlson E., Ferrin T.E.,
Herskowitz I., Giacomini K.M.;
"Evolutionary conservation predicts function of variants of the human
organic cation transporter, OCT1.";
Proc. Natl. Acad. Sci. U.S.A. 100:5902-5907(2003).
[19]
VARIANTS PHE-160; LEU-283; GLY-287 AND LEU-341.
PubMed=14697261; DOI=10.1016/j.bbrc.2003.11.175;
Sakata T., Anzai N., Shin H.J., Noshiro R., Hirata T., Yokoyama H.,
Kanai Y., Endou H.;
"Novel single nucleotide polymorphisms of organic cation transporter 1
(SLC22A1) affecting transport functions.";
Biochem. Biophys. Res. Commun. 313:789-793(2004).
[20]
VARIANTS LEU-41; PHE-160; LEU-341 AND VAL-408.
PubMed=15499200; DOI=10.2133/dmpk.19.308;
Itoda M., Saito Y., Maekawa K., Hichiya H., Komamura K., Kamakura S.,
Kitakaze M., Tomoike H., Ueno K., Ozawa S., Sawada J.;
"Seven novel single nucleotide polymorphisms in the human SLC22A1 gene
encoding organic cation transporter 1 (OCT1).";
Drug Metab. Pharmacokinet. 19:308-312(2004).
-!- FUNCTION: Translocates a broad array of organic cations with
various structures and molecular weights including the model
compounds 1-methyl-4-phenylpyridinium (MPP), tetraethylammonium
(TEA), N-1-methylnicotinamide (NMN), 4-(4-(dimethylamino)styryl)-
N-methylpyridinium (ASP), the endogenous compounds choline,
guanidine, histamine, epinephrine, adrenaline, noradrenaline and
dopamine, and the drugs quinine, and metformin. The transport of
organic cations is inhibited by a broad array of compounds like
tetramethylammonium (TMA), cocaine, lidocaine, NMDA receptor
antagonists, atropine, prazosin, cimetidine, TEA and NMN,
guanidine, cimetidine, choline, procainamide, quinine,
tetrabutylammonium, and tetrapentylammonium. Translocates organic
cations in an electrogenic and pH-independent manner. Translocates
organic cations across the plasma membrane in both directions.
Transports the polyamines spermine and spermidine. Transports
pramipexole across the basolateral membrane of the proximal
tubular epithelial cells. The choline transport is activated by
MMTS. Regulated by various intracellular signaling pathways
including inhibition by protein kinase A activation, and
endogenously activation by the calmodulin complex, the calmodulin-
dependent kinase II and LCK tyrosine kinase.
{ECO:0000269|PubMed:11388889, ECO:0000269|PubMed:11408531,
ECO:0000269|PubMed:15389554, ECO:0000269|PubMed:16272756,
ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:9187257,
ECO:0000269|PubMed:9260930, ECO:0000269|PubMed:9655880}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.47 mM for metformin {ECO:0000269|PubMed:16272756,
ECO:0000269|PubMed:9187257, ECO:0000269|PubMed:9655880};
KM=229 uM for TEA {ECO:0000269|PubMed:16272756,
ECO:0000269|PubMed:9187257, ECO:0000269|PubMed:9655880};
KM=14.6 uM for MPP {ECO:0000269|PubMed:16272756,
ECO:0000269|PubMed:9187257, ECO:0000269|PubMed:9655880};
Vmax=396 pmol/min/mg enzyme for metformin uptake
{ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:9187257,
ECO:0000269|PubMed:9655880};
Vmax=2.89 nmol/min/mg enzyme for TEA uptake
{ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:9187257,
ECO:0000269|PubMed:9655880};
-!- INTERACTION:
Q96G23:CERS2; NbExp=3; IntAct=EBI-1172714, EBI-1057080;
-!- SUBCELLULAR LOCATION: Basolateral cell membrane
{ECO:0000269|PubMed:16263091}; Multi-pass membrane protein
{ECO:0000269|PubMed:16263091}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=hOCT1G/L554;
IsoId=O15245-1; Sequence=Displayed;
Name=2; Synonyms=hOCT1G/L506;
IsoId=O15245-2; Sequence=VSP_033589, VSP_033590;
Name=3; Synonyms=hOCT1G483;
IsoId=O15245-3; Sequence=VSP_033588;
Name=4; Synonyms=hOCT1G353;
IsoId=O15245-4; Sequence=VSP_033587;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- TISSUE SPECIFICITY: Widely expressed with high level in liver.
Isoform 1 and isoform 2 are expressed in liver. Isoform 1, isoform
2, isoform 3 and isoform 4 are expressed in glial cell lines.
{ECO:0000269|PubMed:11388889, ECO:0000269|PubMed:9187257,
ECO:0000269|PubMed:9260930}.
-!- INDUCTION: In the liver activated by HNF4A and suppressed by bile
acids via NR0B2. Increased by cholesterol treatment in hepatocyte
cells. {ECO:0000269|PubMed:16436500, ECO:0000269|PubMed:17635184}.
-!- PTM: Phosphorylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1)
superfamily. Organic cation transporter (TC 2.A.1.19) family.
{ECO:0000305}.
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EMBL; X98332; CAA66977.1; -; mRNA.
EMBL; U77086; AAB67703.1; -; mRNA.
EMBL; AJ243995; CAB95971.1; -; Genomic_DNA.
EMBL; AJ243996; CAB95971.1; JOINED; Genomic_DNA.
EMBL; AJ243998; CAB95971.1; JOINED; Genomic_DNA.
EMBL; AJ243999; CAB95971.1; JOINED; Genomic_DNA.
EMBL; AJ244000; CAB95971.1; JOINED; Genomic_DNA.
EMBL; AJ245460; CAB95971.1; JOINED; Genomic_DNA.
EMBL; AJ276051; CAB95971.1; JOINED; Genomic_DNA.
EMBL; AJ276052; CAB95971.1; JOINED; Genomic_DNA.
EMBL; AJ276053; CAB95971.1; JOINED; Genomic_DNA.
EMBL; AK289887; BAF82576.1; -; mRNA.
EMBL; AL353625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC126364; AAI26365.1; -; mRNA.
CCDS; CCDS5274.1; -. [O15245-1]
CCDS; CCDS5275.1; -. [O15245-2]
RefSeq; NP_003048.1; NM_003057.2. [O15245-1]
RefSeq; NP_694857.1; NM_153187.1. [O15245-2]
RefSeq; XP_006715615.1; XM_006715552.1. [O15245-3]
UniGene; Hs.117367; -.
ProteinModelPortal; O15245; -.
BioGrid; 112467; 1.
IntAct; O15245; 1.
STRING; 9606.ENSP00000355930; -.
BindingDB; O15245; -.
ChEMBL; CHEMBL5685; -.
DrugBank; DB01193; Acebutolol.
DrugBank; DB01614; Acepromazine.
DrugBank; DB03128; Acetylcholine.
DrugBank; DB00787; Aciclovir.
DrugBank; DB08838; Agmatine.
DrugBank; DB00915; Amantadine.
DrugBank; DB00594; Amiloride.
DrugBank; DB00345; Aminohippuric acid.
DrugBank; DB04830; Buformin.
DrugBank; DB00520; Caspofungin.
DrugBank; DB01114; Chlorphenamine.
DrugBank; DB00477; Chlorpromazine.
DrugBank; DB00122; Choline.
DrugBank; DB00501; Cimetidine.
DrugBank; DB00242; Cladribine.
DrugBank; DB00575; Clonidine.
DrugBank; DB00318; Codeine.
DrugBank; DB00987; Cytarabine.
DrugBank; DB04485; Deoxythymidine.
DrugBank; DB01151; Desipramine.
DrugBank; DB09555; Dexchlorpheniramine maleate.
DrugBank; DB00917; Dinoprostone.
DrugBank; DB01075; Diphenhydramine.
DrugBank; DB00280; Disopyramide.
DrugBank; DB00988; Dopamine.
DrugBank; DB00668; Epinephrine.
DrugBank; DB00783; Estradiol.
DrugBank; DB04574; Estrone sulfate.
DrugBank; DB01004; Ganciclovir.
DrugBank; DB00406; Gentian Violet.
DrugBank; DB00536; Guanidine.
DrugBank; DB05381; Histamine.
DrugBank; DB00619; Imatinib.
DrugBank; DB00458; Imipramine.
DrugBank; DB00224; Indinavir.
DrugBank; DB00709; Lamivudine.
DrugBank; DB00654; Latanoprost.
DrugBank; DB00331; Metformin.
DrugBank; DB00683; Midazolam.
DrugBank; DB00220; Nelfinavir.
DrugBank; DB00184; Nicotine.
DrugBank; DB00368; Norepinephrine.
DrugBank; DB00526; Oxaliplatin.
DrugBank; DB01337; Pancuronium.
DrugBank; DB00914; Phenformin.
DrugBank; DB00925; Phenoxybenzamine.
DrugBank; DB01621; Pipotiazine.
DrugBank; DB00413; Pramipexole.
DrugBank; DB00457; Prazosin.
DrugBank; DB01032; Probenecid.
DrugBank; DB01035; Procainamide.
DrugBank; DB00396; Progesterone.
DrugBank; DB00908; Quinidine.
DrugBank; DB00468; Quinine.
DrugBank; DB00863; Ranitidine.
DrugBank; DB00206; Reserpine.
DrugBank; DB00728; Rocuronium.
DrugBank; DB01232; Saquinavir.
DrugBank; DB03566; Spermidine.
DrugBank; DB00127; Spermine.
DrugBank; DB04348; Taurocholic Acid.
DrugBank; DB00624; Testosterone.
DrugBank; DB08837; Tetraethylammonium.
DrugBank; DB00152; Thiamine.
DrugBank; DB01622; Thioproperazine.
DrugBank; DB01623; Thiothixene.
DrugBank; DB01199; Tubocurarine.
DrugBank; DB01339; Vecuronium.
DrugBank; DB00661; Verapamil.
GuidetoPHARMACOLOGY; 1019; -.
TCDB; 2.A.1.19.29; the major facilitator superfamily (mfs).
iPTMnet; O15245; -.
PhosphoSitePlus; O15245; -.
BioMuta; SLC22A1; -.
PaxDb; O15245; -.
PeptideAtlas; O15245; -.
PRIDE; O15245; -.
DNASU; 6580; -.
Ensembl; ENST00000324965; ENSP00000318103; ENSG00000175003. [O15245-2]
Ensembl; ENST00000366963; ENSP00000355930; ENSG00000175003. [O15245-1]
Ensembl; ENST00000457470; ENSP00000409557; ENSG00000175003. [O15245-3]
Ensembl; ENST00000460902; ENSP00000439274; ENSG00000175003. [O15245-4]
GeneID; 6580; -.
KEGG; hsa:6580; -.
UCSC; uc003qtc.4; human. [O15245-1]
CTD; 6580; -.
DisGeNET; 6580; -.
EuPathDB; HostDB:ENSG00000175003.12; -.
GeneCards; SLC22A1; -.
HGNC; HGNC:10963; SLC22A1.
HPA; HPA029846; -.
MIM; 602607; gene.
neXtProt; NX_O15245; -.
OpenTargets; ENSG00000175003; -.
PharmGKB; PA329; -.
eggNOG; KOG0255; Eukaryota.
eggNOG; COG0477; LUCA.
GeneTree; ENSGT00760000118852; -.
HOGENOM; HOG000234568; -.
HOVERGEN; HBG061545; -.
InParanoid; O15245; -.
KO; K08198; -.
OMA; ILMYLWF; -.
OrthoDB; EOG091G05AC; -.
PhylomeDB; O15245; -.
TreeFam; TF315847; -.
Reactome; R-HSA-112311; Neurotransmitter clearance.
Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle.
Reactome; R-HSA-2161517; Abacavir transmembrane transport.
Reactome; R-HSA-442660; Na+/Cl- dependent neurotransmitter transporters.
Reactome; R-HSA-549127; Organic cation transport.
GeneWiki; SLC22A1; -.
GenomeRNAi; 6580; -.
PRO; PR:O15245; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000175003; -.
CleanEx; HS_SLC22A1; -.
ExpressionAtlas; O15245; baseline and differential.
Genevisible; O15245; HS.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
GO; GO:0016020; C:membrane; TAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005277; F:acetylcholine transmembrane transporter activity; IBA:GO_Central.
GO; GO:0005329; F:dopamine transmembrane transporter activity; IBA:GO_Central.
GO; GO:0005333; F:norepinephrine transmembrane transporter activity; IBA:GO_Central.
GO; GO:0008514; F:organic anion transmembrane transporter activity; IBA:GO_Central.
GO; GO:0015101; F:organic cation transmembrane transporter activity; EXP:Reactome.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0015651; F:quaternary ammonium group transmembrane transporter activity; IBA:GO_Central.
GO; GO:0008513; F:secondary active organic cation transmembrane transporter activity; IBA:GO_Central.
GO; GO:0015872; P:dopamine transport; IBA:GO_Central.
GO; GO:0006855; P:drug transmembrane transport; TAS:Reactome.
GO; GO:0048241; P:epinephrine transport; IEA:Ensembl.
GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; IEA:Ensembl.
GO; GO:0006836; P:neurotransmitter transport; IBA:GO_Central.
GO; GO:0015874; P:norepinephrine transport; IBA:GO_Central.
GO; GO:0015695; P:organic cation transport; TAS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
CDD; cd06174; MFS; 1.
InterPro; IPR020846; MFS_dom.
InterPro; IPR005828; MFS_sugar_transport-like.
InterPro; IPR036259; MFS_trans_sf.
InterPro; IPR004749; Orgcat_transp/SVOP.
InterPro; IPR005829; Sugar_transporter_CS.
Pfam; PF00083; Sugar_tr; 2.
SUPFAM; SSF103473; SSF103473; 1.
TIGRFAMs; TIGR00898; 2A0119; 1.
PROSITE; PS50850; MFS; 1.
PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Glycoprotein;
Ion transport; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 554 Solute carrier family 22 member 1.
/FTId=PRO_0000333875.
TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TOPO_DOM 43 149 Extracellular. {ECO:0000255}.
TRANSMEM 150 170 Helical. {ECO:0000255}.
TOPO_DOM 171 176 Cytoplasmic. {ECO:0000255}.
TRANSMEM 177 197 Helical. {ECO:0000255}.
TOPO_DOM 198 206 Extracellular. {ECO:0000255}.
TRANSMEM 207 229 Helical. {ECO:0000255}.
TOPO_DOM 230 235 Cytoplasmic. {ECO:0000255}.
TRANSMEM 236 256 Helical. {ECO:0000255}.
TOPO_DOM 257 262 Extracellular. {ECO:0000255}.
TRANSMEM 263 283 Helical. {ECO:0000255}.
TOPO_DOM 284 347 Cytoplasmic. {ECO:0000255}.
TRANSMEM 348 368 Helical. {ECO:0000255}.
TOPO_DOM 369 376 Extracellular. {ECO:0000255}.
TRANSMEM 377 397 Helical. {ECO:0000255}.
TOPO_DOM 398 402 Cytoplasmic. {ECO:0000255}.
TRANSMEM 403 423 Helical. {ECO:0000255}.
TOPO_DOM 424 431 Extracellular. {ECO:0000255}.
TRANSMEM 432 452 Helical. {ECO:0000255}.
TOPO_DOM 453 464 Cytoplasmic. {ECO:0000255}.
TRANSMEM 465 485 Helical. {ECO:0000255}.
TOPO_DOM 486 492 Extracellular. {ECO:0000255}.
TRANSMEM 493 513 Helical. {ECO:0000255}.
TOPO_DOM 514 554 Cytoplasmic. {ECO:0000255}.
SITE 450 450 Involved in affinity and selectivity of
cations as well as in translocation.
{ECO:0000250}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000250|UniProtKB:O08966}.
MOD_RES 541 541 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 354 554 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_033587.
VAR_SEQ 462 532 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_033588.
VAR_SEQ 462 506 RNLGVMVCSSLCDIGGIITPFIVFRLREVWQALPLILFAVL
GLLA -> SGVGPACRGSDATSSRDQGGRFARDHEGRREPW
EKSKAQRKHDLP (in isoform 2).
{ECO:0000305}.
/FTId=VSP_033589.
VAR_SEQ 507 554 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_033590.
VARIANT 14 14 S -> F (exclusively found in the African
American population; increase of the MPP
uptake when associated with V-408;
dbSNP:rs34447885).
{ECO:0000269|PubMed:12719534}.
/FTId=VAR_043319.
VARIANT 41 41 F -> L (in dbSNP:rs2297373).
{ECO:0000269|PubMed:15499200}.
/FTId=VAR_043320.
VARIANT 61 61 R -> C (affects transporter activity;
reduction of the MPP uptake when
associated with V-408; dbSNP:rs12208357).
{ECO:0000269|PubMed:12439218,
ECO:0000269|PubMed:12719534}.
/FTId=VAR_043321.
VARIANT 85 85 L -> F (no changes in the MPP uptake when
associated with V-408; dbSNP:rs35546288).
{ECO:0000269|PubMed:12719534}.
/FTId=VAR_043322.
VARIANT 88 88 C -> R (in dbSNP:rs55918055).
{ECO:0000269|PubMed:12439218}.
/FTId=VAR_043323.
VARIANT 160 160 L -> F (no changes in both TEA and MPP
uptake; abolishes MPP uptake when
associated with S-401; largely localized
to the plasma membrane; dbSNP:rs683369).
{ECO:0000269|PubMed:12439218,
ECO:0000269|PubMed:12719534,
ECO:0000269|PubMed:14697261,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15499200,
ECO:0000269|PubMed:9260930}.
/FTId=VAR_043324.
VARIANT 189 189 S -> L (no changes in the MPP uptake;
dbSNP:rs34104736).
{ECO:0000269|PubMed:12719534}.
/FTId=VAR_043325.
VARIANT 220 220 G -> V (affects MPP uptake; reduction of
the MPP uptake when associated with V-
408; dbSNP:rs36103319).
{ECO:0000269|PubMed:12719534}.
/FTId=VAR_043326.
VARIANT 283 283 P -> L (in dbSNP:rs4646277).
{ECO:0000269|PubMed:14697261}.
/FTId=VAR_043327.
VARIANT 287 287 R -> G (in dbSNP:rs4646278).
{ECO:0000269|PubMed:14697261}.
/FTId=VAR_043328.
VARIANT 341 341 P -> L (affects transporter activity;
reduction of the TEA uptake; reduction of
the MPP uptake when associated with V-
408; largely localized to the plasma
membrane; dbSNP:rs2282143).
{ECO:0000269|PubMed:12719534,
ECO:0000269|PubMed:14697261,
ECO:0000269|PubMed:15499200}.
/FTId=VAR_043329.
VARIANT 342 342 R -> H (no changes in the MPP uptake when
associated with V-408; dbSNP:rs34205214).
{ECO:0000269|PubMed:12719534}.
/FTId=VAR_043330.
VARIANT 401 401 G -> S (affects transporter activity;
reduction of the serotonin uptake; no MPP
uptake when associated with L-160;
dbSNP:rs34130495).
{ECO:0000269|PubMed:12439218,
ECO:0000269|PubMed:12719534}.
/FTId=VAR_043331.
VARIANT 408 408 M -> V (does not affect transporter
activity; no changes in the MPP uptake
when associated with F-14; no changes in
the MPP uptake when associated with F-85;
no changes in the MPP uptake when
associated with L-189; no changes in the
MPP uptake when associated with His-342;
no changes in the MPP uptake when
associated with M-420 del; no changes in
the MPP uptake when associated with I-
440; no changes in the MPP uptake when
associated with I-461; no changes in the
MPP uptake when associated with M-488;
reduction of the MPP uptake when
associated with C-61; no MPP uptake when
associated with V-220; reduction of the
MPP uptake when associated with L-341; no
MPP uptake when associated with S-401; no
MPP uptake when associated with R-465;
dbSNP:rs628031).
{ECO:0000269|PubMed:12719534,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15499200}.
/FTId=VAR_043332.
VARIANT 420 420 Missing (no changes in the MPP uptake
when associated with V-408).
{ECO:0000269|PubMed:12439218,
ECO:0000269|PubMed:12719534,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_043333.
VARIANT 440 440 M -> I (in dbSNP:rs35956182).
{ECO:0000269|PubMed:12719534}.
/FTId=VAR_043334.
VARIANT 461 461 V -> I (no changes in the MPP uptake when
associated with V-408; dbSNP:rs34295611).
{ECO:0000269|PubMed:12719534}.
/FTId=VAR_043335.
VARIANT 465 465 G -> R (reduction of the localization to
the basolateral membrane; no MPP uptake
when associated with V-408;
dbSNP:rs34059508).
{ECO:0000269|PubMed:12719534,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_043336.
VARIANT 488 488 R -> M (no changes in the MPP uptake when
associated with V-408; dbSNP:rs35270274).
{ECO:0000269|PubMed:12719534}.
/FTId=VAR_043337.
MUTAGEN 465 465 G->A: No changes in the MPP uptake.
{ECO:0000269|PubMed:12719534}.
SEQUENCE 554 AA; 61154 MW; 55206B897DE32202 CRC64;
MPTVDDILEQ VGESGWFQKQ AFLILCLLSA AFAPICVGIV FLGFTPDHHC QSPGVAELSQ
RCGWSPAEEL NYTVPGLGPA GEAFLGQCRR YEVDWNQSAL SCVDPLASLA TNRSHLPLGP
CQDGWVYDTP GSSIVTEFNL VCADSWKLDL FQSCLNAGFL FGSLGVGYFA DRFGRKLCLL
GTVLVNAVSG VLMAFSPNYM SMLLFRLLQG LVSKGNWMAG YTLITEFVGS GSRRTVAIMY
QMAFTVGLVA LTGLAYALPH WRWLQLAVSL PTFLFLLYYW CVPESPRWLL SQKRNTEAIK
IMDHIAQKNG KLPPADLKML SLEEDVTEKL SPSFADLFRT PRLRKRTFIL MYLWFTDSVL
YQGLILHMGA TSGNLYLDFL YSALVEIPGA FIALITIDRV GRIYPMAMSN LLAGAACLVM
IFISPDLHWL NIIIMCVGRM GITIAIQMIC LVNAELYPTF VRNLGVMVCS SLCDIGGIIT
PFIVFRLREV WQALPLILFA VLGLLAAGVT LLLPETKGVA LPETMKDAEN LGRKAKPKEN
TIYLKVQTSE PSGT


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